Literature DB >> 2551998

Sodium channel gating in clonal pituitary cells. The inactivation step is not voltage dependent.

G Cota1, C M Armstrong.   

Abstract

We have determined the time course of Na channel inactivation in clonal pituitary (GH3) cells by comparing records before and after the enzymatic removal of inactivation. The cells were subjected to whole-cell patch clamp, with papain included in the internal medium. Inactivation was slowly removed over the course of 10 min, making it possible to obtain control records before the enzyme acted. Papain caused a large (4-100x) increase in current magnitude for small depolarizations (near -40 mV), and a much smaller increase for large ones (approximately 1.5x at +40 mV). For technical reasons it was sometimes convenient to study outward INa recorded with no Na+ outside. The instantaneous I-V (IIV) curve in this condition was nonlinear before papain, and more nearly linear afterwards. The gNa-V curve after papain, obtained by dividing the INa-V curve by the IIV curve, was left-shifted by at least 20 mV and steepened. A spontaneous 5-10 mV left shift occurred in the absence of papain. The rate of the inactivation step was found to vary only slightly from -100 mV to +60 mV, based on the following evidence. (a) Before papain, inactivation rate saturated with voltage and was constant from +20 to +60 mV. (b) We activated the channels with a brief pulse, and studied the time course of the current on changing the voltage to a second, usually more negative level (Na+ present internally and externally). The time course of inactivation at each voltage was obtained by comparing control traces with those after inactivation was removed. When the 5-10-mV spontaneous shift was taken into account, inactivation rate changed by less than 10% from -100 to +60 mV. The data are considered in terms of existing models of the Na channel.

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Year:  1989        PMID: 2551998      PMCID: PMC2228939          DOI: 10.1085/jgp.94.2.213

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  63 in total

1.  A point mutation in domain 4-segment 6 of the skeletal muscle sodium channel produces an atypical inactivation state.

Authors:  J P O'Reilly; S Y Wang; G K Wang
Journal:  Biophys J       Date:  2000-02       Impact factor: 4.033

2.  L-type calcium channel activity regulates sodium channel levels in rat pituitary GH3 cells.

Authors:  E Monjaraz; A Navarrete; L F Lopez-Santiago; A V Vega; J A Arias-Montaño; G Cota
Journal:  J Physiol       Date:  2000-02-15       Impact factor: 5.182

3.  Membrane stretch affects gating modes of a skeletal muscle sodium channel.

Authors:  I V Tabarean; P Juranka; C E Morris
Journal:  Biophys J       Date:  1999-08       Impact factor: 4.033

4.  Outer and central charged residues in DIVS4 of skeletal muscle sodium channels have differing roles in deactivation.

Authors:  James Groome; Esther Fujimoto; Lisa Walter; Peter Ruben
Journal:  Biophys J       Date:  2002-03       Impact factor: 4.033

5.  Negative charges in the DIII-DIV linker of human skeletal muscle Na+ channels regulate deactivation gating.

Authors:  James R Groome; Esther Fujimoto; Peter C Ruben
Journal:  J Physiol       Date:  2003-02-14       Impact factor: 5.182

6.  Amino acid residues required for fast Na(+)-channel inactivation: charge neutralizations and deletions in the III-IV linker.

Authors:  D E Patton; J W West; W A Catterall; A L Goldin
Journal:  Proc Natl Acad Sci U S A       Date:  1992-11-15       Impact factor: 11.205

7.  Giga-seal formation alters properties of sodium channels of human myoballs.

Authors:  C Fahlke; R Rüdel
Journal:  Pflugers Arch       Date:  1992-03       Impact factor: 3.657

Review 8.  Calcium channels: unanswered questions.

Authors:  Stephen W Jones
Journal:  J Bioenerg Biomembr       Date:  2003-12       Impact factor: 2.945

9.  The quantal gating charge of sodium channel inactivation.

Authors:  N G Greeff; I C Forster
Journal:  Eur Biophys J       Date:  1991       Impact factor: 1.733

10.  Functional modulation of voltage-dependent sodium channel expression by wild type and mutated C121W-β1 subunit.

Authors:  Debora Baroni; Raffaella Barbieri; Cristiana Picco; Oscar Moran
Journal:  J Bioenerg Biomembr       Date:  2013-04-13       Impact factor: 2.945

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